5HJY

Structure function studies of R. palustris RubisCO (I165T mutant; CABP-bound)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	PIXEL
Collection date	2013-08-11
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.9793
Spacegroup name	P 1
Unit cell lengths	73.860, 100.020, 103.560
Unit cell angles	107.84, 113.77, 96.09

Refinement procedure

Resolution	91.850 - 2.300
R-factor	0.187
Rwork	0.183
R-free	0.22500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4lf1
RMSD bond length	0.006
RMSD bond angle	0.844
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	91.850	2.360
High resolution limit [Å]	2.300	2.300
Rmerge	0.114	0.508
Number of reflections	103448
<I/σ(I)>	8.99	2.76
Completeness [%]	93.1	90
Redundancy	3.7	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		291	Protein storage buffer: 20 mM Tris, pH 8.0, 300 mM NaCl, 10% Glycerol, 10 mM MgCl2, 20 mM NaHCO3. Protein concentration: 16 mg/ml. Reservoir solution: 20-24% PEG 3350, 200 mM sodium sulfate, 100 mM Bis-Tris Propane pH 7-8.